Abstract

SummaryIn many organisms, circadian rhythms and associated oscillations in gene expression are controlled by post-translational modifications of histone proteins. Although epigenetic mechanisms influence key aspects of insect societies, their implication in regulating circadian rhythms has not been studied in social insects. Here we ask whether histone acetylation plays a role in adjusting circadian activity in the ant Temnothorax longispinosus. We characterized activity patterns in 20 colonies to reveal that these ants exhibit a diurnal rhythm in colony-level activity and can rapidly respond to changes in the light regime. Then we fed T. longispinosus colonies with C646, a chemical inhibitor of histone acetyltransferases, to show that treated colonies lost their circadian rhythmicity and failed to adjust their activity to the light regime. These findings suggest a role for histone acetylation in controlling rhythmicity in ants and implicate epigenetic processes in the regulation of circadian rhythms in a social context.

Highlights

  • The rotation of the earth around the sun causes daily rhythmicity in environmental conditions

  • SUMMARY In many organisms, circadian rhythms and associated oscillations in gene expression are controlled by post-translational modifications of histone proteins

  • Epigenetic mechanisms influence key aspects of insect societies, their implication in regulating circadian rhythms has not been studied in social insects

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Summary

Introduction

The rotation of the earth around the sun causes daily rhythmicity in environmental conditions. Most animal cells can maintain rhythmic processes and metabolic activities, the synchronization between the organisms’ rhythm and external cues (e.g., light) is typically controlled and maintained by the circadian clock, which acts as a central pacemaker in the brain (Mendoza-Viveros et al, 2017; Takahashi, 2017). The circadian clock is a set of conserved proteins that interact to regulate daily oscillations in gene expression and protein production (Mendoza-Viveros et al, 2017). The CLOCK protein is central to the molecular clock, as it forms a heterodimer with BMAL1 (in mammals) or CYCLE (in flies) and acts as a transcription factor that drives downstream transcriptional changes by binding to enhancer-boxes (E-boxes) in the promoter region of other clock genes (Bell-Pedersen et al, 2005). Molecular clock activity results in large-scale downstream changes in gene expression (Zhang et al, 2014) that may involve less targeted gene regulatory routes (Takahashi, 2017)

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